ATS19_HUMAN
ID ATS19_HUMAN Reviewed; 1207 AA.
AC Q8TE59;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 19;
DE Short=ADAM-TS 19;
DE Short=ADAM-TS19;
DE Short=ADAMTS-19;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAMTS19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11867212; DOI=10.1016/s0378-1119(01)00861-7;
RA Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C.;
RT "Cloning, expression analysis, and structural characterization of seven
RT novel human ADAMTSs, a family of metalloproteinases with disintegrin and
RT thrombospondin-1 domains.";
RL Gene 283:49-62(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-360.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal lung, but not in any adult
CC tissues examined. Expression was detected in an osteosarcoma cDNA
CC library.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
CC threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-
CC G of the TSP type-1 repeat domains where C1 and C2 are the first and
CC second cysteine residue of the repeat, respectively. Fucosylated
CC repeats can then be further glycosylated by the addition of a beta-1,3-
CC glucose residue by the glucosyltransferase, B3GALTL. Fucosylation
CC mediates the efficient secretion of ADAMTS family members. Can also be
CC C-glycosylated with one or two mannose molecules on tryptophan residues
CC within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated.
CC These other glycosylations can also facilitate secretion (By
CC similarity). {ECO:0000250}.
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DR EMBL; AJ311904; CAC84565.1; -; mRNA.
DR EMBL; AC008425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_598377.4; NM_133638.4.
DR AlphaFoldDB; Q8TE59; -.
DR SMR; Q8TE59; -.
DR BioGRID; 128101; 2.
DR IntAct; Q8TE59; 1.
DR STRING; 9606.ENSP00000274487; -.
DR MEROPS; M12.029; -.
DR GlyGen; Q8TE59; 5 sites.
DR iPTMnet; Q8TE59; -.
DR PhosphoSitePlus; Q8TE59; -.
DR BioMuta; ADAMTS19; -.
DR DMDM; 296434402; -.
DR EPD; Q8TE59; -.
DR MassIVE; Q8TE59; -.
DR PaxDb; Q8TE59; -.
DR PeptideAtlas; Q8TE59; -.
DR PRIDE; Q8TE59; -.
DR ProteomicsDB; 74401; -.
DR DNASU; 171019; -.
DR GeneID; 171019; -.
DR KEGG; hsa:171019; -.
DR UCSC; uc003kvb.2; human.
DR CTD; 171019; -.
DR DisGeNET; 171019; -.
DR GeneCards; ADAMTS19; -.
DR HGNC; HGNC:17111; ADAMTS19.
DR MIM; 607513; gene.
DR neXtProt; NX_Q8TE59; -.
DR PharmGKB; PA24545; -.
DR eggNOG; KOG3538; Eukaryota.
DR HOGENOM; CLU_000660_8_1_1; -.
DR InParanoid; Q8TE59; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q8TE59; -.
DR TreeFam; TF313537; -.
DR PathwayCommons; Q8TE59; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q8TE59; -.
DR BioGRID-ORCS; 171019; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; ADAMTS19; human.
DR GenomeRNAi; 171019; -.
DR Pharos; Q8TE59; Tbio.
DR PRO; PR:Q8TE59; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q8TE59; protein.
DR Genevisible; Q8TE59; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..316
FT /evidence="ECO:0000250"
FT /id="PRO_0000029202"
FT CHAIN 317..1207
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 19"
FT /id="PRO_0000029203"
FT DOMAIN 325..545
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 546..633
FT /note="Disintegrin"
FT DOMAIN 634..686
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 915..975
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 976..1037
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1039..1083
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1087..1144
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1160..1199
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 49..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..914
FT /note="Spacer"
FT MOTIF 292..299
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 95..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 401..466
FT /evidence="ECO:0000250"
FT DISULFID 441..448
FT /evidence="ECO:0000250"
FT DISULFID 460..540
FT /evidence="ECO:0000250"
FT DISULFID 499..524
FT /evidence="ECO:0000250"
FT DISULFID 569..593
FT /evidence="ECO:0000250"
FT DISULFID 580..601
FT /evidence="ECO:0000250"
FT DISULFID 588..620
FT /evidence="ECO:0000250"
FT DISULFID 614..625
FT /evidence="ECO:0000250"
FT DISULFID 645..680
FT /evidence="ECO:0000250"
FT DISULFID 649..685
FT /evidence="ECO:0000250"
FT DISULFID 660..670
FT /evidence="ECO:0000250"
FT DISULFID 988..1031
FT /evidence="ECO:0000250"
FT DISULFID 992..1036
FT /evidence="ECO:0000250"
FT DISULFID 1003..1020
FT /evidence="ECO:0000250"
FT VARIANT 360
FT /note="L -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036154"
FT VARIANT 582
FT /note="E -> G (in dbSNP:rs10062501)"
FT /id="VAR_057087"
FT VARIANT 1089
FT /note="Y -> F (in dbSNP:rs11749126)"
FT /id="VAR_024599"
FT CONFLICT 367
FT /note="S -> G (in Ref. 1; CAC84565)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048
FT /note="C -> F (in Ref. 1; CAC84565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1207 AA; 134048 MW; 21EFB26660DEB6D9 CRC64;
MRLTHICCCC LLYQLGFLSN GIVSELQFAP DREEWEVVFP ALWRREPVDP AGGSGGSADP
GWVRGVGGGG SARAQAAGSS REVRSVAPVP LEEPVEGRSE SRLRPPPPSE GEEDEELESQ
ELPRGSSGAA ALSPGAPASW QPPPPPQPPP SPPPAQHAEP DGDEVLLRIP AFSRDLYLLL
RRDGRFLAPR FAVEQRPNPG PGPTGAASAP QPPAPPDAGC FYTGAVLRHP GSLASFSTCG
GGLMGFIQLN EDFIFIEPLN DTMAITGHPH RVYRQKRSME EKVTEKSALH SHYCGIISDK
GRPRSRKIAE SGRGKRYSYK LPQEYNIETV VVADPAMVSY HGADAARRFI LTILNMVFNL
FQHKSLSVQV NLRVIKLILL HETPPELYIG HHGEKMLESF CKWQHEEFGK KNDIHLEMST
NWGEDMTSVD AAILITRKDF CVHKDEPCDT VGIAYLSGMC SEKRKCIIAE DNGLNLAFTI
AHEMGHNMGI NHDNDHPSCA DGLHIMSGEW IKGQNLGDVS WSRCSKEDLE RFLRSKASNC
LLQTNPQSVN SVMVPSKLPG MTYTADEQCQ ILFGPLASFC QEMQHVICTG LWCKVEGEKE
CRTKLDPPMD GTDCDLGKWC KAGECTSRTS APEHLAGEWS LWSPCSRTCS AGISSRERKC
PGLDSEARDC NGPRKQYRIC ENPPCPAGLP GFRDWQCQAY SVRTSSPKHI LQWQAVLDEE
KPCALFCSPV GKEQPILLSE KVMDGTSCGY QGLDICANGR CQKVGCDGLL GSLAREDHCG
VCNGNGKSCK IIKGDFNHTR GAGYVEVLVI PAGARRIKVV EEKPAHSYLA LRDAGKQSIN
SDWKIEHSGA FNLAGTTVHY VRRGLWEKIS AKGPTTAPLH LLVLLFQDQN YGLHYEYTIP
SDPLPENQSS KAPEPLFMWT HTSWEDCDAT CGGGERKTTV SCTKIMSKNI SIVDNEKCKY
LTKPEPQIRK CNEQPCQTRW MMTEWTPCSR TCGKGMQSRQ VACTQQLSNG TLIRARERDC
IGPKPASAQR CEGQDCMTVW EAGVWSECSV KCGKGIRHRT VRCTNPRKKC VLSTRPREAE
DCEDYSKCYV WRMGDWSKCS ITCGKGMQSR VIQCMHKITG RHGNECFSSE KPAAYRPCHL
QPCNEKINVN TITSPRLAAL TFKCLGDQWP VYCRVIREKN LCQDMRWYQR CCETCRDFYA
QKLQQKS
